Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyClass II glutamine amidotransferases8064070 3000131 SCOP2B (2022-06-29)
V [auth O]SCOP2B SuperfamilyClass II glutamine amidotransferases8064070 3000131 SCOP2B (2022-06-29)
LSCOP2B SuperfamilyClass II glutamine amidotransferases8079498 3000131 SCOP2B (2022-06-29)
X [auth Z]SCOP2B SuperfamilyClass II glutamine amidotransferases8079498 3000131 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyClass II glutamine amidotransferases8064034 3000131 SCOP2B (2022-06-29)
W [auth P]SCOP2B SuperfamilyClass II glutamine amidotransferases8064034 3000131 SCOP2B (2022-06-29)
AA [auth Q]SCOP2B SuperfamilyClass II glutamine amidotransferases8064028 3000131 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyClass II glutamine amidotransferases8064028 3000131 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyClass II glutamine amidotransferases8064032 3000131 SCOP2B (2022-06-29)
S [auth R]SCOP2B SuperfamilyClass II glutamine amidotransferases8064032 3000131 SCOP2B (2022-06-29)
ESCOP2B SuperfamilyClass II glutamine amidotransferases8064024 3000131 SCOP2B (2022-06-29)
O [auth S]SCOP2B SuperfamilyClass II glutamine amidotransferases8064024 3000131 SCOP2B (2022-06-29)
FSCOP2B SuperfamilyClass II glutamine amidotransferases8064064 3000131 SCOP2B (2022-06-29)
TSCOP2B SuperfamilyClass II glutamine amidotransferases8064064 3000131 SCOP2B (2022-06-29)
BA [auth U]SCOP2B SuperfamilyClass II glutamine amidotransferases8064068 3000131 SCOP2B (2022-06-29)
GSCOP2B SuperfamilyClass II glutamine amidotransferases8064068 3000131 SCOP2B (2022-06-29)
ISCOP2B SuperfamilyClass II glutamine amidotransferases8064072 3000131 SCOP2B (2022-06-29)
U [auth W]SCOP2B SuperfamilyClass II glutamine amidotransferases8064072 3000131 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AProteasomee6muwA1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
V [auth O]Proteasomee6muwO1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
P [auth X]Proteasomee6muwX1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
JProteasomee6muwJ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
KProteasomee6muwK1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
Q [auth Y]Proteasomee6muwY1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
LProteasomee6muwL1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
X [auth Z]Proteasomee6muwZ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
MProteasomee6muwM1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
Y [auth a]Proteasomee6muwa1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
NProteasomee6muwN1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
R [auth b]Proteasomee6muwb1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BProteasomee6muwB1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
W [auth P]Proteasomee6muwP1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
AA [auth Q]Proteasomee6muwQ1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
CProteasomee6muwC1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
DProteasomee6muwD1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
S [auth R]Proteasomee6muwR1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
EProteasomee6muwE1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
O [auth S]Proteasomee6muwS1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
FProteasomee6muwF1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
TProteasomee6muwT1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
BA [auth U]Proteasomee6muwU1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
GProteasomee6muwG1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
HProteasomee6muwH1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
Z [auth V]Proteasomee6muwV1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
IProteasomee6muwI1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)
U [auth W]Proteasomee6muwW1 A: a+b four layersX: Ntn/PP2CH: NtnT: Proteasome subunitsF: ProteasomeECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
V [auth O]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
P [auth X]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
J3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
K3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
Q [auth Y]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
L3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
X [auth Z]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
M3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
Y [auth a]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
N3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
R [auth b]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
B3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
W [auth P]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
AA [auth Q]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
C3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
D3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
S [auth R]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
E3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
O [auth S]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
F3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
T3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
BA [auth U]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
G3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
H3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
Z [auth V]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
I3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)
U [auth W]3.60.20.10 Alpha Beta 4-Layer Sandwich Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 Aminohydrolase, N-terminal nucleophile (Ntn) domainCATH (utative)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A,
V [auth O]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
A,
V [auth O]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
J,
P [auth X]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
K,
Q [auth Y]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
L,
X [auth Z]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
N,
R [auth b]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
B,
W [auth P]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
B,
W [auth P]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
AA [auth Q],
C
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
AA [auth Q],
C
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
D,
S [auth R]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
D,
S [auth R]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
E,
O [auth S]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
E,
O [auth S]
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
F, T
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
F, T
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
BA [auth U],
G
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
BA [auth U],
G
PF10584Proteasome subunit A N-terminal signature (Proteasome_A_N)Proteasome subunit A N-terminal signature- Family
H,
Z [auth V]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain
I,
U [auth W]
PF00227Proteasome subunit (Proteasome)Proteasome subunitThe proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity ...The proteasome is a multisubunit structure that degrades proteins. Protein degradation is an essential component of regulation because proteins can become misfolded, damaged, or unnecessary. Proteasomes and their homologues vary greatly in complexity: from HslV (heat shock locus v), which is encoded by 1 gene in bacteria, to the eukaryotic 20S proteasome, which is encoded by more than 14 genes [1]. Recently evidence of two novel groups of bacterial proteasomes was proposed. The first is Anbu, which is sparsely distributed among cyanobacteria and proteobacteria [1]. The second is call beta-proteobacteria proteasome homologue (BPH) [1].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A,
V [auth O]
20S proteasome alpha-1 subunit
J,
P [auth X]
20S proteasome beta-3 subunit
K,
Q [auth Y]
20S proteasome beta-4 subunit
L,
X [auth Z]
20S proteasome beta-5 subunit
M,
Y [auth a]
20S proteasome beta-6 subunit---
N,
R [auth b]
20S proteasome beta-7 subunit
B,
W [auth P]
20S proteasome alpha-2 subunit
AA [auth Q],
C
20S proteasome alpha-3 subunit
D,
S [auth R]
20S proteasome alpha-4 subunit
E,
O [auth S]
20S proteasome alpha-5 subunit
F, T
20S proteasome alpha-6 subunit
BA [auth U],
G
20S proteasome alpha-7 subunit
H,
Z [auth V]
20S proteasome beta-1 subunit
I,
U [auth W]
20S proteasome beta-2 subunit

InterPro: Protein Family Classification InterPro Database Homepage

ChainsAccessionNameType
A,
V [auth O]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
A,
V [auth O]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
A,
V [auth O]
IPR023332Proteasome alpha-type subunitFamily
A,
V [auth O]
IPR001353Proteasome, subunit alpha/betaFamily
A,
V [auth O]
IPR034642Proteasome subunit alpha6Family
J,
P [auth X]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
J,
P [auth X]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
J,
P [auth X]
IPR023333Proteasome B-type subunitFamily
J,
P [auth X]
IPR001353Proteasome, subunit alpha/betaFamily
J,
P [auth X]
IPR033811Proteasome beta 3 subunitFamily
K,
Q [auth Y]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
K,
Q [auth Y]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
K,
Q [auth Y]
IPR001353Proteasome, subunit alpha/betaFamily
K,
Q [auth Y]
IPR035206Proteasome subunit beta 2Family
L,
X [auth Z]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
L,
X [auth Z]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
L,
X [auth Z]
IPR023333Proteasome B-type subunitFamily
L,
X [auth Z]
IPR001353Proteasome, subunit alpha/betaFamily
L,
X [auth Z]
IPR000243Peptidase T1A, proteasome beta-subunitFamily
N,
R [auth b]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
N,
R [auth b]
IPR023333Proteasome B-type subunitFamily
N,
R [auth b]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
N,
R [auth b]
IPR016295Proteasome subunit beta 4Family
N,
R [auth b]
IPR001353Proteasome, subunit alpha/betaFamily
B,
W [auth P]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
B,
W [auth P]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
B,
W [auth P]
IPR023332Proteasome alpha-type subunitFamily
B,
W [auth P]
IPR001353Proteasome, subunit alpha/betaFamily
AA [auth Q],
C
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
AA [auth Q],
C
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
AA [auth Q],
C
IPR023332Proteasome alpha-type subunitFamily
AA [auth Q],
C
IPR001353Proteasome, subunit alpha/betaFamily
D,
S [auth R]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
D,
S [auth R]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
D,
S [auth R]
IPR023332Proteasome alpha-type subunitFamily
D,
S [auth R]
IPR001353Proteasome, subunit alpha/betaFamily
E,
O [auth S]
IPR033812Proteasome subunit alpha5Family
E,
O [auth S]
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
E,
O [auth S]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
E,
O [auth S]
IPR023332Proteasome alpha-type subunitFamily
E,
O [auth S]
IPR001353Proteasome, subunit alpha/betaFamily
F, T
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
F, T
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
F, T
IPR035144Proteasome subunit alpha 1Family
F, T
IPR023332Proteasome alpha-type subunitFamily
F, T
IPR001353Proteasome, subunit alpha/betaFamily
BA [auth U],
G
IPR000426Proteasome alpha-subunit, N-terminal domainDomain
BA [auth U],
G
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
BA [auth U],
G
IPR001353Proteasome, subunit alpha/betaFamily
H,
Z [auth V]
IPR023333Proteasome B-type subunitFamily
H,
Z [auth V]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
H,
Z [auth V]
IPR001353Proteasome, subunit alpha/betaFamily
I,
U [auth W]
IPR016050Proteasome beta-type subunit, conserved siteConserved Site
I,
U [auth W]
IPR029055Nucleophile aminohydrolases, N-terminalHomologous Superfamily
I,
U [auth W]
IPR023333Proteasome B-type subunitFamily
I,
U [auth W]
IPR001353Proteasome, subunit alpha/betaFamily
I,
U [auth W]
IPR000243Peptidase T1A, proteasome beta-subunitFamily